Abstract
Mammalian liver peroxisomes contain only one kind of aminotransferase, alanine:glyoxylate aminotransferase 1 (AGT 1). Hepatic organelles containing AGT 1 and its substrate specificity vary among mammalian. AGT 1 is located in peroxisomes in human, monkey, rabbit and guinea-pig, in the mitochondria in dog and cat, and in both organelles in rat, mouse and hamster. Rodent AGT 1 catalyze the transamination between various L-amino acids and pyruvate or glyoxylate, while other mammalian AGT 1 have only AGT and serine:pyruvate aminotransferase activities. Immunological distances of AGT 1 in different organelles from different mammalian species suggest that the peroxisomal and mitochondrial AGT 1 were orthologous proteins, and were not formed by divergent evolution after gene duplication. AGT 1 is present as the holoenzyme in mammalian liver, while AGT is present as the apoenzyme in chicken and chick embryonic liver. Furthermore, some evidence that animal peroxisomes play a role in detoxication of glyoxylate is presented.
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Noguchi, T. (1987). Amino Acid Metabolism in Animal Peroxisomes. In: Fahimi, H.D., Sies, H. (eds) Peroxisomes in Biology and Medicine. Proceedings in Life Sciences. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-71325-5_23
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DOI: https://doi.org/10.1007/978-3-642-71325-5_23
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